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  1. Article: We Don't Have to Lose STEM Students to Business.

    Wernick, Naomi L B / Ledley, Fred D

    Journal of microbiology & biology education

    2020  Volume 21, Issue 1

    Abstract: Most undergraduate students who leave STEM majors before graduation choose careers in business. This article argues that better integrating business opportunities and context into the STEM curriculum could advance STEM learning, motivate students to ... ...

    Abstract Most undergraduate students who leave STEM majors before graduation choose careers in business. This article argues that better integrating business opportunities and context into the STEM curriculum could advance STEM learning, motivate students to remain in STEM as majors, and cultivate a constructive relationship between business, science, and society.
    Language English
    Publishing date 2020-04-30
    Publishing country United States
    Document type Journal Article
    ISSN 1935-7877
    ISSN 1935-7877
    DOI 10.1128/jmbe.v21i1.2095
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: We Don’t Have to Lose STEM Students to Business

    Naomi L. B. Wernick / Fred D. Ledley

    Journal of Microbiology & Biology Education, Vol 21, Iss

    2020  Volume 1

    Abstract: Most undergraduate students who leave STEM majors before graduation choose careers in business. This article argues that better integrating business opportunities and context into the STEM curriculum could advance STEM learning, motivate students to ... ...

    Abstract Most undergraduate students who leave STEM majors before graduation choose careers in business. This article argues that better integrating business opportunities and context into the STEM curriculum could advance STEM learning, motivate students to remain in STEM as majors, and cultivate a constructive relationship between business, science, and society.
    Keywords Special aspects of education ; LC8-6691 ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2020-01-01T00:00:00Z
    Publisher American Society for Microbiology
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article: Positioning genomics in biology education: content mapping of undergraduate biology textbooks.

    Wernick, Naomi L B / Ndung'u, Eric / Haughton, Dominique / Ledley, Fred D

    Journal of microbiology & biology education

    2014  Volume 15, Issue 2, Page(s) 268–276

    Abstract: Biological thought increasingly recognizes the centrality of the genome in constituting and regulating processes ranging from cellular systems to ecology and evolution. In this paper, we ask whether genomics is similarly positioned as a core concept in ... ...

    Abstract Biological thought increasingly recognizes the centrality of the genome in constituting and regulating processes ranging from cellular systems to ecology and evolution. In this paper, we ask whether genomics is similarly positioned as a core concept in the instructional sequence for undergraduate biology. Using quantitative methods, we analyzed the order in which core biological concepts were introduced in textbooks for first-year general and human biology. Statistical analysis was performed using self-organizing map algorithms and conventional methods to identify clusters of terms and their relative position in the books. General biology textbooks for both majors and nonmajors introduced genome-related content after text related to cell biology and biological chemistry, but before content describing higher-order biological processes. However, human biology textbooks most often introduced genomic content near the end of the books. These results suggest that genomics is not yet positioned as a core concept in commonly used textbooks for first-year biology and raises questions about whether such textbooks, or courses based on the outline of these textbooks, provide an appropriate foundation for understanding contemporary biological science.
    Language English
    Publishing date 2014-12-15
    Publishing country United States
    Document type Journal Article
    ISSN 1935-7877
    ISSN 1935-7877
    DOI 10.1128/jmbe.v15i2.724
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Positioning Genomics in Biology Education

    Naomi L. B. Wernick / Eric Ndung'u / Dominique Haughton / Fred D. Ledley

    Journal of Microbiology & Biology Education, Vol 15, Iss

    Content Mapping of Undergraduate Biology Textbooks

    2014  Volume 2

    Abstract: Biological thought increasingly recognizes the centrality of the genome in constituting and regulating processes ranging from cellular systems to ecology and evolution. In this paper, we ask whether genomics is similarly positioned as a core concept in ... ...

    Abstract Biological thought increasingly recognizes the centrality of the genome in constituting and regulating processes ranging from cellular systems to ecology and evolution. In this paper, we ask whether genomics is similarly positioned as a core concept in the instructional sequence for undergraduate biology. Using quantitative methods, we analyzed the order in which core biological concepts were introduced in textbooks for first-year general and human biology. Statistical analysis was performed using self-organizing map algorithms and conventional methods to identify clusters of terms and their relative position in the books. General biology textbooks for both majors and nonmajors introduced genome-related content after text related to cell biology and biological chemistry, but before content describing higher-order biological processes. However, human biology textbooks most often introduced genomic content near the end of the books. These results suggest that genomics is not yet positioned as a core concept in commonly used textbooks for first-year biology and raises questions about whether such textbooks, or courses based on the outline of these textbooks, provide an appropriate foundation for understanding contemporary biological science.
    Keywords undergraduate biology ; genomics ; content map ; Kohonen Self-Organizing Maps ; biology curriculum ; textbooks ; Special aspects of education ; LC8-6691 ; Biology (General) ; QH301-705.5
    Subject code 501 ; 070
    Language English
    Publishing date 2014-07-01T00:00:00Z
    Publisher American Society for Microbiology
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Positioning Genomics in Biology Education

    Naomi L. B. Wernick / Eric Ndung’u / Dominique Haughton / Fred D. Ledley

    Journal of Microbiology & Biology Education, Vol 15, Iss 2, Pp 268-

    Content Mapping of Undergraduate Biology Textbooks

    2014  Volume 276

    Abstract: Biological thought increasingly recognizes the centrality of the genome in constituting and regulating processes ranging from cellular systems to ecology and evolution. In this paper, we ask whether genomics is similarly positioned as a core concept in ... ...

    Abstract Biological thought increasingly recognizes the centrality of the genome in constituting and regulating processes ranging from cellular systems to ecology and evolution. In this paper, we ask whether genomics is similarly positioned as a core concept in the instructional sequence for undergraduate biology. Using quantitative methods, we analyzed the order in which core biological concepts were introduced in textbooks for first-year general and human biology. Statistical analysis was performed using self-organizing map algorithms and conventional methods to identify clusters of terms and their relative position in the books. General biology textbooks for both majors and nonmajors introduced genome-related content after text related to cell biology and biological chemistry, but before content describing higher-order biological processes. However, human biology textbooks most often introduced genomic content near the end of the books. These results suggest that genomics is not yet positioned as a core concept in commonly used textbooks for first-year biology and raises questions about whether such textbooks, or courses based on the outline of these textbooks, provide an appropriate foundation for understanding contemporary biological science.
    Keywords Special aspects of education ; LC8-6691 ; Biology (General) ; QH301-705.5
    Subject code 070
    Language English
    Publishing date 2014-12-01T00:00:00Z
    Publisher American Society for Microbiology
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article: N-terminal Extension of the Cholera Toxin A1-chain Causes Rapid Degradation after Retrotranslocation from Endoplasmic Reticulum to Cytosol

    Wernick, Naomi L.B / De Luca, Heidi / Kam, Wendy R / Lencer, Wayne I

    Journal of biological chemistry. 2010 Feb. 26, v. 285, no. 9

    2010  

    Abstract: Cholera toxin travels from the plasma membrane to the endoplasmic reticulum of host cells, where a portion of the toxin, the A1-chain, is unfolded and targeted to a protein-conducting channel for retrotranslocation to the cytosol. Unlike most ... ...

    Abstract Cholera toxin travels from the plasma membrane to the endoplasmic reticulum of host cells, where a portion of the toxin, the A1-chain, is unfolded and targeted to a protein-conducting channel for retrotranslocation to the cytosol. Unlike most retrotranslocation substrates, the A1-chain escapes degradation by the proteasome and refolds in the cytosol to induce disease. How this occurs remains poorly understood. Here, we show that an unstructured peptide appended to the N terminus of the A1-chain renders the toxin functionally inactive. Cleavage of the peptide extension prior to cell entry rescues toxin half-life and function. The loss of toxicity is explained by rapid degradation by the proteasome after retrotranslocation to the cytosol. Degradation of the mutant toxin does not follow the N-end rule but depends on the two Lys residues at positions 4 and 17 of the native A1-chain, consistent with polyubiquitination at these sites. Thus, retrotranslocation and refolding of the wild-type A1-chain must proceed in a way that protects these Lys residues from attack by E3 ligases.
    Language English
    Dates of publication 2010-0226
    Size p. 6145-6152.
    Publishing place American Society for Biochemistry and Molecular Biology
    Document type Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    Database NAL-Catalogue (AGRICOLA)

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  7. Article ; Online: Cholera toxin: an intracellular journey into the cytosol by way of the endoplasmic reticulum.

    Wernick, Naomi L B / Chinnapen, Daniel J-F / Cho, Jin Ah / Lencer, Wayne I

    Toxins

    2010  Volume 2, Issue 3, Page(s) 310–325

    Abstract: Cholera toxin (CT), an AB(5)-subunit toxin, enters host cells by binding the ganglioside GM1 at the plasma membrane (PM) and travels retrograde through the trans-Golgi Network into the endoplasmic reticulum (ER). In the ER, a portion of CT, the enzymatic ...

    Abstract Cholera toxin (CT), an AB(5)-subunit toxin, enters host cells by binding the ganglioside GM1 at the plasma membrane (PM) and travels retrograde through the trans-Golgi Network into the endoplasmic reticulum (ER). In the ER, a portion of CT, the enzymatic A1-chain, is unfolded by protein disulfide isomerase and retro-translocated to the cytosol by hijacking components of the ER associated degradation pathway for misfolded proteins. After crossing the ER membrane, the A1-chain refolds in the cytosol and escapes rapid degradation by the proteasome to induce disease by ADP-ribosylating the large G-protein Gs and activating adenylyl cyclase. Here, we review the mechanisms of toxin trafficking by GM1 and retro-translocation of the A1-chain to the cytosol.
    MeSH term(s) Cell Membrane/metabolism ; Cholera Toxin/chemistry ; Cholera Toxin/metabolism ; Cytosol/metabolism ; Endoplasmic Reticulum/metabolism ; G(M1) Ganglioside/metabolism ; Humans ; Protein Conformation ; Protein Transport
    Chemical Substances G(M1) Ganglioside (37758-47-7) ; Cholera Toxin (9012-63-9)
    Language English
    Publishing date 2010-03-05
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2518395-3
    ISSN 2072-6651 ; 2072-6651
    ISSN (online) 2072-6651
    ISSN 2072-6651
    DOI 10.3390/toxins2030310
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: N-terminal extension of the cholera toxin A1-chain causes rapid degradation after retrotranslocation from endoplasmic reticulum to cytosol.

    Wernick, Naomi L B / De Luca, Heidi / Kam, Wendy R / Lencer, Wayne I

    The Journal of biological chemistry

    2010  Volume 285, Issue 9, Page(s) 6145–6152

    Abstract: Cholera toxin travels from the plasma membrane to the endoplasmic reticulum of host cells, where a portion of the toxin, the A1-chain, is unfolded and targeted to a protein-conducting channel for retrotranslocation to the cytosol. Unlike most ... ...

    Abstract Cholera toxin travels from the plasma membrane to the endoplasmic reticulum of host cells, where a portion of the toxin, the A1-chain, is unfolded and targeted to a protein-conducting channel for retrotranslocation to the cytosol. Unlike most retrotranslocation substrates, the A1-chain escapes degradation by the proteasome and refolds in the cytosol to induce disease. How this occurs remains poorly understood. Here, we show that an unstructured peptide appended to the N terminus of the A1-chain renders the toxin functionally inactive. Cleavage of the peptide extension prior to cell entry rescues toxin half-life and function. The loss of toxicity is explained by rapid degradation by the proteasome after retrotranslocation to the cytosol. Degradation of the mutant toxin does not follow the N-end rule but depends on the two Lys residues at positions 4 and 17 of the native A1-chain, consistent with polyubiquitination at these sites. Thus, retrotranslocation and refolding of the wild-type A1-chain must proceed in a way that protects these Lys residues from attack by E3 ligases.
    MeSH term(s) Animals ; Chlorocebus aethiops ; Cholera Toxin/chemistry ; Cholera Toxin/genetics ; Cholera Toxin/metabolism ; Cytosol/metabolism ; Endoplasmic Reticulum/metabolism ; Half-Life ; Lysine ; Peptides/pharmacology ; Proteasome Endopeptidase Complex/metabolism ; Protein Conformation ; Protein Folding ; Protein Stability ; Protein Transport ; Ubiquitin-Protein Ligases/metabolism ; Vero Cells
    Chemical Substances Peptides ; Cholera Toxin (9012-63-9) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2010-01-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M109.062067
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Recognition of the tryptophan-based endocytosis signal in the neonatal Fc Receptor by the mu subunit of adaptor protein-2.

    Wernick, Naomi L B / Haucke, Volker / Simister, Neil E

    The Journal of biological chemistry

    2004  Volume 280, Issue 8, Page(s) 7309–7316

    Abstract: Endocytosis of membrane proteins is typically mediated by signals present in their cytoplasmic domains. These signals usually contain an essential tyrosine or pair of leucine residues. Both tyrosine- and dileucine-based endocytosis signals are recognized ...

    Abstract Endocytosis of membrane proteins is typically mediated by signals present in their cytoplasmic domains. These signals usually contain an essential tyrosine or pair of leucine residues. Both tyrosine- and dileucine-based endocytosis signals are recognized by the adaptor complex AP-2. The best understood of these interactions occurs between the tyrosine-based motif, YXXPhi, and the mu2 subunit of AP-2. We recently reported a tryptophan-based endocytosis signal, WLSL, contained within the cytoplasmic domain of the neonatal Fc receptor. This signal resembles YXXPhi. We have investigated the mechanism by which the tryptophan-based signal is recognized. Both interaction assays in vitro and endocytosis assays in vivo show that mu2 binds the tryptophan-based signal. Furthermore, the WLSL sequence binds the same site as YXXPhi. Unlike the WXXF motif, contained in stonin 2 and other endocytic proteins, WLSL does not bind the alpha subunit of AP-2. These observations reveal a functional similarity between the tryptophan-based endocytosis signal and the YXXPhi motif, and an unexpected versatility of mu2 function.
    MeSH term(s) Adaptor Protein Complex 2/metabolism ; Adaptor Protein Complex 2/physiology ; Adaptor Protein Complex mu Subunits/metabolism ; Adaptor Protein Complex mu Subunits/physiology ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Line ; Endocytosis ; Histocompatibility Antigens Class I ; Protein Binding ; Rats ; Receptors, Fc/metabolism ; Signal Transduction ; Transfection ; Tryptophan
    Chemical Substances Adaptor Protein Complex 2 ; Adaptor Protein Complex mu Subunits ; Histocompatibility Antigens Class I ; Receptors, Fc ; adaptor protein complex 2, mu 2 subunit ; Tryptophan (8DUH1N11BX) ; Fc receptor, neonatal (TW3XAW0RCY)
    Language English
    Publishing date 2004-12-14
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M410752200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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